Rationally designed helical peptidomimetics disrupt α-synuclein fibrillation-Reference-Cited by-同舟云学术

Rationally designed helical peptidomimetics disrupt α-synuclein fibrillation

Published:2022 Issue:33 Volume:58 Page:5132-5135
ISSN:1359-7345
Container-title:Chemical Communications
language:en
Short-container-title:Chem. Commun.

Author:

Bavinton Clementine E.¹,Sternke-Hoffmann Rebecca²,Yamashita Tohru³,Knipe Peter C.³⁴^ORCID,Hamilton Andrew D.³⁵^ORCID,Luo Jinghui²^ORCID,Thompson Sam¹³^ORCID

Affiliation:

1. School of Chemistry and the Institute for Life Sciences, University of Southampton, Southampton, SO17 1BJ, UK

2. Paul Scherrer Institute, Forschungsstrasse 111, 5232 Villigen PSI, Switzerland

3. Department of Chemistry, University of Oxford, Oxford, OX1 3TA, UK

4. School of Chemistry and Chemical Engineering, Queen's University Belfast, David Keir Building, Belfast, BT9 5AG, UK

5. Department of Chemistry, New York University, 100 Washington Square East, NY 10003, USA

Abstract

Misfolding of the human protein α-synuclein results in toxic fibrils, which are a hallmark of Parkinson's disease. Herein we show that structure-guided rationally designed peptidomimetics drastically slow the rate of protein aggregation.

Funder

Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung

Engineering and Physical Sciences Research Council

Brightfocus Foundation

Paul Scherrer Institute

Publisher

Royal Society of Chemistry (RSC)

Subject

Materials Chemistry,Metals and Alloys,Surfaces, Coatings and Films,General Chemistry,Ceramics and Composites,Electronic, Optical and Magnetic Materials,Catalysis

Link

http://pubs.rsc.org/en/content/articlepdf/2022/CC/D2CC00212D

Reference36 articles.

1. Lewy pathology in Parkinson’s disease consists of crowded organelles and lipid membranes

2. Structure and Dynamics of Micelle-bound Human α-Synuclein

3. Structure of membrane-bound -synuclein from site-directed spin labeling and computational refinement

4. α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation

5. Mutations associated with familial Parkinson’s disease alter the initiation and amplification steps of α-synuclein aggregation

Cited by 19 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Phase Separation and Aggregation of α‐Synuclein Diverge at Different Salt Conditions;Advanced Science;2024-07-07

2. Protein mimetic 2D FAST rescues alpha synuclein aggregation mediated early and post disease Parkinson’s phenotypes;Nature Communications;2024-04-30

3. Phase Separation and Aggregation of α-Synuclein Diverge at Different Salt Conditions;2024-03-03

4. Oncogenic R248W mutation induced conformational perturbation of the p53 core domain and the structural protection by proteomimetic amyloid inhibitor ADH-6;Physical Chemistry Chemical Physics;2024

5. Exploring Peptido‐Nanocomposites in the Context of Amyloid Diseases;Angewandte Chemie International Edition;2023-11-22